This is indicative of the stability of the complex around the NPs due to their interaction with stabilizing proteins at these later time points.
In addition, electrochemical studies provide an insight into the stability of the complex.
The mutations also improve the stability of the complex with cognate DNA.
One is the electrostatic attraction between the central cation and the negative point charges, which is largely responsible for the stability of the complex.
Mainly the interaction between OH groups of PVA and iodine has been found to determine the stability of the complex.
Free-energy calculations demonstrate the stability of the complex and help identify key residues in various interactions based on residue decomposition analysis.
When the ligand or the protein is modified so that the stability of the complex is decreased, biological activity is impaired.
We have analyzed the stability of the complex and characterized its interactions at the atomic level by performing free energy calculations and computational alanine scanning.
The stability of the complex was further supported by root mean square fluctuation (RMSF), beta factor and radius of gyration values.
Properties of interest include the stability of the complex under physiological conditions and how the complex will interact with biological macromolecules including proteins, genetic material, and polysaccharides.
The presented work allowed for recognition of different types of interactions, as well as for the calculation of association constants that demonstrate the stability of the complex.
